We have previously found that elongation factor-2 (EF-2) has differing subcellular distribution in intact HeLa cells corresponding to differing growth conditions of the cell such as amino acid deprivation. EF-2 is found as part of a large multi-translation enzyme aggregate with other enzymes such as EF-1, various aminoacyl tRNA synthetases and initiation factors. The unit complex may be associated with subribosomal particles of distinct morphology. In order to better understand the physiological significance of these enzymes with the normal and malignant human cells, we plan to investigate both the 1) chemical and 2) biological properties of the complex by the following route: 1. Chemical Characterization and Purification; a) purification of complex and electron microscopy of particles. b) GTP binding to complexed EF-2. c) reconstitution of components of complex. d and e) RNA and poly A analysis of complex. 2. Biological Significance of Intact HeLa Cells of Translational Enzymes Associated with Cell Particulate; a) ribosome binding studies. b) high molecular weight forms of enzymes and cell stress-- amino acid deprivation. c) complex and selective restriction of protein synthesis by contact inhibition, membrane alterations, and antibiotics. d) release of complex from polyribosomes. e) relationship to oncogenic viral translation. f) high molecular weight EF-2 amd ppGpp. g) initiation of translation and complex.